Q5AQA6 · LP9E_EMENI

Function

function

Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H2O2 or O2 as a cosubstrate (Probable).

Catalytic activity

  • [(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + acceptor + H2O.
    EC:1.14.99.56 (UniProtKB | ENZYME | Rhea)

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 1 copper ion per subunit.

Biotechnology

Lignocellulose is the most abundant polymeric composite on Earth and is a recalcitrant but promising renewable substrate for industrial biotechnology applications. Together with cellobiose dehydrogenases (CDHs) an enzymatic system capable of oxidative cellulose cleavage is formed, which increases the efficiency of cellulases and put LPMOs at focus of biofuel research.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site17Cu2+ (UniProtKB | ChEBI); catalytic
Binding site102Cu2+ (UniProtKB | ChEBI); catalytic
Binding site180O2 (UniProtKB | ChEBI)
Binding site189O2 (UniProtKB | ChEBI)
Binding site191Cu2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncellulase activity
Molecular Functioncellulose binding
Molecular Functionmetal ion binding
Molecular Functionmonooxygenase activity
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • AA9Auxiliary Activities 9
    • CBM1Carbohydrate-Binding Module Family 1

Names & Taxonomy

Protein names

  • Recommended name
    AA9 family lytic polysaccharide monooxygenase E
  • EC number
  • Short names
    LPMO9E
  • Alternative names
    • Cellulase LPMO9E
    • Endo-beta-1,4-glucanase LPMO9E
      (Endoglucanase LPMO9E
      )
    • Glycosyl hydrolase 61 family protein LPMO9E

Gene names

    • Name
      LPMO9E
    • ORF names
      AN9524, ANIA_09524

Organism names

Accessions

  • Primary accession
    Q5AQA6
  • Secondary accessions
    • C8VI93

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-16
ChainPRO_501017922417-402AA9 family lytic polysaccharide monooxygenase E
Disulfide bond72↔194
Glycosylation75N-linked (GlcNAc...) asparagine
Disulfide bond113↔117
Glycosylation154N-linked (GlcNAc...) asparagine

Keywords

Expression

Induction

Expression is significantly induced by xylan and slightly induce by cellulose (PubMed:27075737).
The degenerate binding motif 5'-SYGGRG-3' that binds to creA involved in carbon catabolite repression is present in the promoter (PubMed:27075737).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain364-400CBM1

Domain

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    402
  • Mass (Da)
    40,494
  • Last updated
    2005-04-26 v1
  • Checksum
    8A71FE2F40F9D6E7
MSRLVSFASLLAAVNAHGYVQNIVVNGVYYSGWEINTYPYMTDPPVVAAWQIPNSNGPVDVSNGYTTEDIICNLNATNAAGYVEVAAGDKINLQWSAWPDTHHGPVISYLADCGDDCTTVDKTTLEFFKIDAVGLVDDSTVPGTWGDDELIENNNSWMVEIPTSIAPGNYVLRHEIIALHSAGTEGGAQNYPQCFNLKVTGSGTDSPAGTLGTELYNLDDPGILVNIYASLSTYVIPGPTLYSGATSIAQATSAITATGSATSGAGGAAATGSSAATTTAAAASTTATPTTAAAQTAKSASAPSSAATGSVPAAPTTATVSTTTSIATSVGTTLTRTTLATTTTAAAAEPSASAPAPSGNSASGSNPLYAQCGGLNFKGASGCVAGATCKKMNPYYSQCVSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BN001306
EMBL· GenBank· DDBJ
CBF83171.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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